issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

November 2014 issue

Highlighted illustration

Cover illustration: Ovine [beta]-lactoglobulin at atomic resolution (Kontopidis et al., p. 1498).

IYCr crystallization series


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Strategies and procedures for the optimization of macromolecular crystal-growth conditions are surveyed. The objective of optimization is to grow crystals with the greatest degree of perfection and that yield the most accurate and precise X-ray diffraction data.

structural communications


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Adenylate kinases play a critical role in intercellular homeostasis by the interconversion of ATP and AMP to two ADP molecules. Crystal structures of adenylate kinase from Streptococcus pneumoniae D39 (SpAdK) have been determined in ligand-free and inhibitor-bound states at 1.96 and 1.65 Å resolution, respectively.

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The structure of the methanofuran/methanopterin-biosynthetic enzyme (MJ1099) from M. jannaschii was determined at 1.7 Å resolution using anomalous scattering methods.

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This article reports the structure of pectin methylesterase from rice weevil (Sitophilus oryzae) which is the first structure of an animal pectin methylesterase.

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The recombinant production and structural analysis of catalytically active type II dehydroquinase from P. aeruginosa are presented.

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The crystal structure of the RNA chaperone Hfq in complex with RNA is presented at 0.97 Å resolution.

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The 1.12 Å resolution crystal structure of a triclinic form of β-lactoglobulin without ligand from the domestic sheep (O. aries) is reported.

crystallization communications


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A crystallization screen was set up for GαsAHD in complex with the specifically selected nanobody CA9177. A high-resolution (1.59 Å) data set was collected for one of the crystallization conditions.

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NADP-dependent glutamate dehydrogenase from A. niger has been crystallized and its preliminary X-ray diffraction analysis at 2.9 Å resolution is reported.

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The cloning, expression, purification, crystallization and preliminary X-ray data collection of allantoinase from B. licheniformis (AllBali) are presented.

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TcdA, a recently characterized E. coli tRNA N6-threonylcarbamoyladenosine dehydratase, previously called CsdL or YgdL, was crystallized in space group P21. Diffraction data were collected to 2.70 Å resolution using synchrotron radiation.

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The protein ccTIM is an engineered variant of the triosephosphate isomerase (TIM) enzyme and has sequence features from both prokaryotic and eukaryotic members of the TIM protein family. Moreover, it is as active as a native protein despite sharing some biophysical characteristics with a molten globular variant. This inscrutable protein was crystallized using the microbatch method and a full X-ray diffraction data set was collected to 2.2 Å resolution using a synchrotron-radiation source.

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The great cormorant hemoglobin has been isolated, purified and crystallized and the three dimensional structure is solved using molecular replacement technique.

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β-Galactosidase from A. niger has been expressed in S. cerevisiae, purified and crystallized in its deglycosylated form. X-ray data have been collected to 1.8 Å resolution.

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VHH R303 binds the Listeria virulence factor InlB. Crystals of R303 were obtained following in situ proteolysis with trypsin. Trypsin removed the flexible tag region of the protein, creating a homogeneous protein preparation. The crystals diffracted to 1.3 Å resolution.

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Gliomedin has an extracellular domain which mediates interactions between the myelinating Schwann cell and the axonal surface, and plays a role in the development and maintenance of the nodes of Ranvier. Here, the purification and crystallization of this olfactomedin domain are reported.

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drFrnE, a disulfide oxidoreductase from D. radiodurans, was crystallized and preliminary diffraction data were obtained. The crystal belonged to space group P21221 and diffracted to 1.8 Å resolution.

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The flagellar accessory protein FlaH from M. jannaschii has been purified and crystallized. The crystal structure has been solved using the MAD method.

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A novel vapour-diffusion crystallization approach was utilized to produce crystals of the enzyme 4-hydroxy-2-oxoglutarate aldolase. This `microtitration' method incorporated ammonium sulfate titration, a miniaturization of the working volume (<10 µl) and a controlled rate of evaporation by utilizing a large reservoir, and yielded crystals with favourable diffraction parameters compared with crystals obtained using the conventional hanging-drop method.

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The cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of PdxK from P. falciparum are described.

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An L-amino-acid oxidase from L. muta venom was crystallized and diffraction data were collected to 3.0 Å resolution.

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The hypothetical deaminase RPB_0146 from R. palustris HaA2 was expressed in E. coli and purified. Crystallization and preliminarily X-ray crystallographic analysis of the recombinant deaminase were performed.

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Thermophilic S-adenosylhomocysteine hydrolase (SAHH) from Thermotoga maritima (TmSAHH), which catalyzes the reversible conversion of S-adenosylhomocysteine into adenosine and homocysteine, was expressed in Escherichia coli and crystallized.

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The PhaA protein from R. eutropha, the first enzyme in the polyhydroxybutyrate biosynthetic pathway, was crystallized and X-ray crystallographic analysis was performed.

laboratory communications


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Rational mutagenesis of the latency-associated nuclear antigen residues 1008–1146 from Kaposi's sarcoma herpesvirus has allowed its crystallization in complex with DNA. A complete data set has been collected at room temperature at a synchrotron-radiation source.
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